Free Standard AU & NZ Shipping For All Book Orders Over $80!
Register      Login
Australian Journal of Chemistry Australian Journal of Chemistry Society
An international journal for chemical science
RESEARCH FRONT

Enzyme Electrochemistry

H. Allen O. Hill A
+ Author Affiliations
- Author Affiliations

A Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, UK. Email: allen.hill@chemistry.oxford.ac.uk




Allen Hill, Emeritus Professor at the University of Oxford and Emeritus Fellow of The Queen's College, Oxford, is the author of more than 400 papers and patents. He obtained his Ph.D. from Queen's University, Belfast. After a number of fellowships he was elected to a lectureship in inorganic chemistry in 1965. In 1977 he first achieved the direct electrochemistry of redox proteins and this developed into a new method of using enzyme electrodes. During the 1980s he achieved the first direct electrochemistry of an enzyme. In 2000, he with three colleagues started Oxford Biosensors where he now works as Director of Strategic Technologies. He has been awarded numerous prizes including the Mullard Prize of the Royal Society, of which he is a Fellow, the Robinson Medal of the RSC, and the Breyer Medal of the RACI.

Australian Journal of Chemistry 59(4) 231-232 https://doi.org/10.1071/CH06120
Submitted: 9 April 2006  Accepted: 9 April 2006   Published: 1 May 2006


References


[1]   P. V. Bernhardt, Aust. J. Chem. 2006, 59,  233.
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
         
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
         
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  
        | Crossref |  GoogleScholarGoogle Scholar |  open url image1




* It is adequate to think of the rate of electron transfer as a function of intervening distance rather than requiring a special electron-transfer path.

It is important to realize that the ‘static’ view of enzyme structures available from diffraction studies could be misleading, in that dynamic motion of or within the protein could bring the prosthetic group within striking distance of the electrode surface.